Two curiously complementary and impeding truisms face any newly proposed concept or outlook in science. They may be demonstrated by two quotations. The first, attributed to Maurice Maeterlinck, indicates the struggle of those who would make new proposals, “At every crossway on the road that leads to the future, tradition, has placed against each of us, 10,000 men to guard the past.” The second suggests why it is so easy, even for those without a direct personal stake, to hold with tradition, “Keep in mind that new ideas are commonplace, and almost always wrong” (E.O. Wilson, Consilience: The Unity of Knowledge, Alfred E. Knopf, New York, 1998). Accordingly, to stand against a new idea is to be almost always right, with neither intellectual effort nor actual understanding required. Those who might practice default to pretense could seldom find a better opportunity.Google Scholar

6.

Webster’s Third New International Dictionary of the English Language, Unabridged, Merriam-Webster, Inc., Springfield, MA, 1993, p. 557.Google Scholar

C.B. Anfinsen, “Principles that Govern the Folding of Protein Chains.” Science, 181, 223–230, 1973; The, Anfinsen principle is that the sequence of a protein dictates the full three-dimensional structure that it would form, that is, sequence dictates protein folding and assembly. The need for molecular chaperones suggests that the correctly folded protein, the lowest energy structure, is not always the result and that the problem arises out of improper hydrophobic associations. Interestingly, the need for molecular chaperones is greatest when temperature is elevated. They were first identified as heat shock proteins, which are just the conditions where metastable hydrophobic associations would occur. The rise in temperature from that of the cusp of insolubility to the insoluble hydrophobically associated state occurred without opportunity for the protein to sort out the lowest energy, hydrophobically associated state. Thus, biology employs a polar cage that ensures hydrophobic dissociation and then systematically decreases polarity of the cage by hydrolysis of ATP with phosphate release to allow for correct hydrophobic re-association.PubMedCrossRefGoogle Scholar